摘要
在生理pH值条件下用荧光光谱和紫外吸收光谱研究了十二烷基苯磺酸钠(SDBS)与牛血清白蛋白(BSA)的相互作用。SDBS可以使BSA的内源荧光发生猝灭,其猝灭机理为静态猝灭。在所研究的浓度范围内获取了SDBS与BSA的结合常数(298K:1.52×105L/mol;310K:7.96×104L/mol)及对应温度下结合反应的热力学参数(ΔH=-41.78kJ/mol;ΔS=-41.00J(/mol·K)/-40.95J(/mol·K);ΔG=-29.56kJ/mol/-29.08kJ/mol)。根据热力学参数推断二者之间的作用力主要为氢键和范德华力。同步荧光光谱表明SDBS的存在改变了BSA的分子构象,BSA分子内的色氨酸残基疏水环境增强。
Binding interaction between sodium dodecylbenzene sulfonate （SDBS） and bovine serum albumin （BSA） was studied by fluorescence and absorption spectroscopy in physiological conditions. Results showed that fluorescence of BSA was quenched by SDBS, and the quenching mechanism was static. Binding constants and thermodynamic parameters were obtained at different temperatures. Main binding force was hydrogen bonds and Van der waals. Results of, synchronous fluorescence spectra indicated that conformation of BSA was changed and hydrophobicity near tryptophan residues were increased at the presence of SDBS.
出处
《环境科学与技术》
CAS
CSCD
北大核心
2009年第1期23-26,共4页
Environmental Science & Technology
基金
辽宁省教育厅项目(20060687)
关键词
十二烷基苯磺酸钠
牛血清白蛋白
相互作用
sodium dodecylbenzene sulfonate（SDBS）
bovine serum albumin（BSA）
interaction
